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3.A.5.1.1
General secretory pathway (Sec-SRP) complex.  A biphasic pulling force may act on TMSs during translocon-mediated membrane integration (Ismail et al. 2012).  Intermediate structures for the insertion of integral membrane proteins have been visualized (Bischoff et al. 2014).  Insertion of the Type II single span (N-terminus, in, C-terminus, out) protein, RodZ, requires only SecYEG, SecA and the pmf, but not SecB, SecDF, YidC or FtsY (Rawat et al. 2015).  The combined effects of ribosome and peptide binding to SecYEG may allow for co-translational membrane insertion of successive transmembrane segments (Ge et al. 2014). SecA penetrates deeply into the SecYEG channel during insertion, contacting transmembrane helices and periplasmic loops (Banerjee et al. 2017). A partially inserted nascent chain unzips the Sec translocon's lateral gate (Kater et al. 2019). Cardiolipin (CL) is required in vivo for the stability of the bacterial translocon (SecYEG) as well as its efficient function in co-translational insertion into and translocation across the inner membrane of E. coli (Ryabichko et al. 2020). PpiD (623 aas and 1 N-terminal TMS), a peptidyl-prolyl cis-trans isomerase D, and YfgM (206 aas and 1 N-terminal TMS) facilitate the transport of toxins into the E. coli cell in a SecY-dependent process (Jones et al. 2021). Synchronized real-time measurement of Sec-mediated protein translocation has been described (Gupta et al. 2021). An extracellular cutinase from Amycolatopsis mediterranei (AmCut) is able to degrade the plastics, polycaprolactone and polybutylene succinate (Tan et al. 2022). It is secreted from E. coli using the Sec system for export across the inner membrane, and possibly, a non-classical secretion pathway for export across the outer membrane (Tan et al. 2022).

Accession Number:P0AG96
Protein Name:Preprotein translocase subunit secE aka prlG aka B3981
Length:127
Molecular Weight:13643.00
Species:Escherichia coli [83333]
Number of TMSs:3
Location1 / Topology2 / Orientation3: Cell inner membrane1 / Multi-pass membrane protein2
Substrate protein polypeptide chain

Cross database links:

RefSeq: AP_003838.1    NP_418408.1   
Entrez Gene ID: 948486   
Pfam: PF00584   
BioCyc: EcoCyc:SECE    ECOL168927:B3981-MONOMER   
KEGG: ecj:JW3944    eco:b3981   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0015450 F:P-P-bond-hydrolysis-driven protein transmem...
GO:0065002 P:intracellular protein transmembrane transport
GO:0009306 P:protein secretion
GO:0006605 P:protein targeting
GO:0043952 P:protein transport by the Sec complex

References (10)

[1] “The secE gene encodes an integral membrane protein required for protein export in Escherichia coli.”  Schatz P.J.et.al.   2673920
[2] “Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon.”  Downing W.L.et.al.   2137819
[3] “Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.”  Blattner F.R.et.al.   8265357
[4] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[5] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[6] “One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.”  Schatz P.J.et.al.   2050112
[7] “Evaluating the oligomeric state of SecYEG in preprotein translocase.”  Yahr T.L.et.al.   10944122
[8] “SecYEG assembles into a tetramer to form the active protein translocation channel.”  Manting E.H.et.al.   10698927
[9] “Global topology analysis of the Escherichia coli inner membrane proteome.”  Daley D.O.et.al.   15919996
[10] “The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE.”  Flower A.M.et.al.   7889938
Structure:
2AKH   2AKI   3J45   3J46   5GAE   5MG3   5NCO   6R7L     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSANTEAQGS GRGLEAMKWV VVVALLLVAI VGNYLYRDIM LPLRALAVVI LIAAAGGVAL 
61:	LTTKGKATVA FAREARTEVR KVIWPTRQET LHTTLIVAAV TAVMSLILWG LDGILVRLVS 
121:	FITGLRF